ID I3D8T0_9PAST Unreviewed; 1148 AA.
AC I3D8T0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Transcription-repair-coupling factor {ECO:0000256|HAMAP-Rule:MF_00969};
DE Short=TRCF {ECO:0000256|HAMAP-Rule:MF_00969};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00969};
GN Name=mfd {ECO:0000256|HAMAP-Rule:MF_00969,
GN ECO:0000313|EMBL:EIJ68123.1};
GN ORFNames=HMPREF1052_1269 {ECO:0000313|EMBL:EIJ68123.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ68123.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ68123.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ68123.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Couples transcription and DNA repair by recognizing RNA
CC polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent
CC release of RNAP and its truncated transcript from the DNA, and
CC recruitment of nucleotide excision repair machinery to the damaged
CC site. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the helicase family.
CC RecG subfamily. {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UvrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00969}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIJ68123.1}.
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DR EMBL; AJSX01000040; EIJ68123.1; -; Genomic_DNA.
DR RefSeq; WP_005761343.1; NZ_AJSX01000040.1.
DR AlphaFoldDB; I3D8T0; -.
DR PATRIC; fig|1095749.3.peg.1744; -.
DR eggNOG; COG1197; Bacteria.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000006457; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0000716; P:transcription-coupled nucleotide-excision repair, DNA damage recognition; IEA:UniProtKB-UniRule.
DR CDD; cd17991; DEXHc_TRCF; 1.
DR CDD; cd18810; SF2_C_TRCF; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.11140; -; 1.
DR Gene3D; 3.40.50.11180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR Gene3D; 3.90.1150.50; Transcription-repair-coupling factor, D7 domain; 1.
DR HAMAP; MF_00969; TRCF; 1.
DR InterPro; IPR003711; CarD-like/TRCF_RID.
DR InterPro; IPR036101; CarD-like/TRCF_RID_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004576; Mfd.
DR InterPro; IPR048635; MFD_D3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047112; RecG/Mfd.
DR InterPro; IPR037235; TRCF-like_C_D7.
DR InterPro; IPR005118; TRCF_C.
DR InterPro; IPR041471; UvrB_inter.
DR NCBIfam; TIGR00580; mfd; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF02559; CarD_TRCF_RID; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21132; MFD_D3; 1.
DR Pfam; PF03461; TRCF; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM01058; CarD_TRCF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00982; TRCF; 1.
DR SUPFAM; SSF141259; CarD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF143517; TRCF domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00969};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00969};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00969};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00969}; Reference proteome {ECO:0000313|Proteomes:UP000006457}.
FT DOMAIN 619..780
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 802..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1148 AA; 130798 MW; 52EAD61129CD7130 CRC64;
MTQTYFNLDI PSQANDHKII GNVIAGSDSL AIAEIASEHK GLTLVVTNDT KSAVKLEKIL
QDISPHEVRY FPDWETLPYD SFSPHQDIIS TRLSTLFYLQ NAKQGIVLLP MTTLMQRVCP
PSYLQHNVLL IKKGDRLVID KLRLQLENAG YRAVEQVLEH GEYAVRGALL DLFPMGSNEP
YRLDFFDDEI DTIRTFDVDT QRTIADINSI NLLPAHEFPT DDKSIEFFRS QFRETFGEIR
RDPEHIYQQV SKGTLVSGIE YWQPLFFEEM ATLFDYLPAN TLFVDMEQTQ IQAERFYQDA
SQRFESRRVD PMRPLLPPER LWLRINEINK ALKNYPRISF KVEKVRSSAR QKNLSVQALP
ELQIQSQQKE PLQNLRQFIE RFKGHIVFSV ETEGRRETLL DLLSPIKLRP QQIENLSQIE
GLNYSLQISS LDNGFIIESE NNEAIAIICE TELLGERVQQ RSRDKRKSVN PDTLIRNLAE
LKIGQAVVHL EHGVGRYGGL VSLENGGIKA EYLLLTYANE AKLYVPVASL HLISRYVGGS
DETAPLHKLG SDAWVKARHK AAEKIRDVAA ELLDVYAQRE AQKGFSFKYD RDEFMQFSAT
FPFEETYDQE LAINAVISDM CQPKAMDRLV CGDVGFGKTE VAMRAAFLSV MNHKQVAVLV
PTTLLAQQHY ENFRDRFANL PVNVEMVSRF RTAKEQKQIL IDLAEGKVDI LIGTHKLIQS
DVRFKDLGLL VIDEEHRFGV RQKEKIKQLR ANIDILTLTA TPIPRTLNMA MNGIRDLSII
STPPARRLTI KTFVRQNDDL VVREAILREI LRGGQVYYLH NDVATIDRCA EKLAELVPEA
RIVVGHGQMH ERELERVMTD FYHQRFNVLV CSTIIETGID VPTANTIIIE RADNFGLAQL
HQLRGRVGRS HHQAYAYLLT PPPKLMTKDA QKRLEALESL DNLGAGFILA THDLEIRGAG
ELLGSEQSGQ IESIGFSLYM ELLESAVKAM KEGREPSLDE LTQQQVEIDL RMPALLPEDY
LGDVNMRLSF YKRIAGAENK ASLDELKVEL IDRFGLLPEA TKNLMQIAEL RLMAKQLGII
RIDGTLHGGF IEFSPTADLD PIKFLNLIKQ QPAVFKFDGP TKFRFTCNLE ENTKRLEFIS
QLVESLLN
//
